Binding of lectins to Streptococcus mitis cells. Studies of the specificity of ligand mediated aggregation.

Previous studies have shown that the mechanism of spontaneous aggregation of Streptococcus mitis ATCC 903 depends on a lectin-ligand type interaction. To study the specificity of the ligand, the binding of a number of lectins of different sugar specificities to the surface of untreated, trypsin and beta-galactosidase-treated bacteria was studied by assessing aggregation. Untreated bacteria were rapidly aggregated by concanavalin A (Con A), wheat-germ agglutination (WGA) and helix pomatia lectin (HPL). Other lectins tested, e.g. peanut agglutinin and soy bean lectin, did not induce aggregation. Lectin-induced aggregation was distinguished from the spontaneous one by recording the course of aggregation and inhibition of lectins by specific sugars. Trypsin-treated bacteria lost their ability for both spontaneous and lectin-induced aggregation. beta-galactosidase-treated bacteria were aggregated only in the presence of Con A and HPL. The bacteria retained their ability for spontaneous aggregation after removal of lectins and inhibitory sugars. These findings suggest that ligand is of glycoprotein nature, since it was removed from the bacterial surface by treatment with trypsin, as shown by the inability of treated cells for both spontaneous and lectin-induced aggregation. Partial degradation of the carbohydrate part of the ligand is indicated by the ability of beta-galactosidase-treated bacteria to aggregate in the presence of Con A and HPL.